ID GLGA_NITEU Reviewed; 495 AA. AC Q82SP3; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 106. DE RecName: Full=Glycogen synthase {ECO:0000255|HAMAP-Rule:MF_00484}; DE EC=2.4.1.21 {ECO:0000255|HAMAP-Rule:MF_00484}; DE AltName: Full=Starch [bacterial glycogen] synthase {ECO:0000255|HAMAP-Rule:MF_00484}; GN Name=glgA {ECO:0000255|HAMAP-Rule:MF_00484}; OrderedLocusNames=NE2264; OS Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC OS 14298). OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosomonas. OX NCBI_TaxID=228410; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298; RX PubMed=12700255; DOI=10.1128/jb.185.9.2759-2773.2003; RA Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L., RA Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A., RA Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.; RT "Complete genome sequence of the ammonia-oxidizing bacterium and obligate RT chemolithoautotroph Nitrosomonas europaea."; RL J. Bacteriol. 185:2759-2773(2003). CC -!- FUNCTION: Synthesizes alpha-1,4-glucan chains using ADP-glucose. CC {ECO:0000255|HAMAP-Rule:MF_00484}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)- CC alpha-D-glucosyl](n+1) + ADP + H(+); Xref=Rhea:RHEA:18189, Rhea:RHEA- CC COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444, CC ChEBI:CHEBI:57498, ChEBI:CHEBI:456216; EC=2.4.1.21; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00484}; CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00484}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. CC Bacterial/plant glycogen synthase subfamily. {ECO:0000255|HAMAP- CC Rule:MF_00484}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL954747; CAD86176.1; -; Genomic_DNA. DR RefSeq; WP_011112755.1; NC_004757.1. DR AlphaFoldDB; Q82SP3; -. DR SMR; Q82SP3; -. DR STRING; 228410.NE2264; -. DR CAZy; GT5; Glycosyltransferase Family 5. DR KEGG; neu:NE2264; -. DR eggNOG; COG0297; Bacteria. DR HOGENOM; CLU_009583_18_2_4; -. DR OrthoDB; 9808590at2; -. DR PhylomeDB; Q82SP3; -. DR UniPathway; UPA00164; -. DR Proteomes; UP000001416; Chromosome. DR GO; GO:0033201; F:alpha-1,4-glucan synthase activity; IEA:UniProtKB-EC. DR GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:InterPro. DR GO; GO:0009011; F:starch synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd03791; GT5_Glycogen_synthase_DULL1-like; 1. DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2. DR HAMAP; MF_00484; Glycogen_synth; 1. DR InterPro; IPR001296; Glyco_trans_1. DR InterPro; IPR011835; GS/SS. DR InterPro; IPR013534; Starch_synth_cat_dom. DR NCBIfam; TIGR02095; glgA; 1. DR PANTHER; PTHR45825; GRANULE-BOUND STARCH SYNTHASE 1, CHLOROPLASTIC/AMYLOPLASTIC; 1. DR PANTHER; PTHR45825:SF11; STARCH SYNTHASE 1, CHLOROPLASTIC_AMYLOPLASTIC; 1. DR Pfam; PF08323; Glyco_transf_5; 1. DR Pfam; PF00534; Glycos_transf_1; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1. PE 3: Inferred from homology; KW Glycogen biosynthesis; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1..495 FT /note="Glycogen synthase" FT /id="PRO_0000188625" FT BINDING 24 FT /ligand="ADP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:57498" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00484" SQ SEQUENCE 495 AA; 54721 MW; A365FB891C2A685D CRC64; MSSSPSRKNP RVLFVTSEVF PLCKTGGLGD VSAALPAALR ELKADVRLLV PGYPSVLSGL KYKRKLAEFD LLPHFPPTTL FSSRLQINES VSLPLYVIHC PELYQRPGGI YLDDDGQDWP DNAQRFGLLS KMGALLASDA SPLSWIPDII HCNDWQSGLT PAYLHYHSGK KAASLMTLHN LAFQGCFPPD EVARLGLPPE SFSVHGVEYY GNLSFLKAGI YYATRITTVS PTYAREIQHE PLGFGLQGLL AERSNAITGI INGIDNTVWN PATDPHIVKK YSSRNLAAKK INKLALQREM GLEENETIPL FAGISRLSYQ KGYDILLQVA PMLADLPAQL VLLGKGDQSL EKQLVMLAQT NPARIAVRID YDEALSHRIN ASADCFLMPS RFEPCGLNQM YSQRYGTPPI VHTTGGLIDT VTDLAPDTPA GESASGFHFH EMTADAFMNG IGRAIDAYYN TRLWKTLQHN GMRKDFSWRS SALAYLSIYS LLMQR //